Novel hydroxamic acid-related phosphinates: inhibition of neutral aminopeptidase N (APN)

Bioorg Med Chem Lett. 2007 Mar 15;17(6):1516-9. doi: 10.1016/j.bmcl.2007.01.028. Epub 2007 Jan 19.

Abstract

Here we describe the inhibitory activity toward neutral aminopeptidase of three new families of phosphinate inhibitors related in structure to hydroxamic acids. These compounds, even as racemic mixtures, are good inhibitors of APN and show strong structure activity relationship (SAR) depending on the substituents in P1 and P1' positions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding, Competitive / drug effects
  • CD13 Antigens / antagonists & inhibitors*
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / pharmacology*
  • Hydroxamic Acids / chemical synthesis*
  • Hydroxamic Acids / pharmacology*
  • Kinetics
  • Metalloproteases / antagonists & inhibitors
  • Phosphinic Acids / chemical synthesis*
  • Phosphinic Acids / pharmacology*
  • Protease Inhibitors / chemical synthesis
  • Protease Inhibitors / pharmacology
  • Stereoisomerism

Substances

  • Enzyme Inhibitors
  • Hydroxamic Acids
  • Phosphinic Acids
  • Protease Inhibitors
  • Metalloproteases
  • CD13 Antigens